• Journal of Ginseng Research
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• v.13 no.2
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• pp.254-259
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• 1989

A radioprotective ginseng protein fraction was obtained from Korean white ginseng powder by the following isolation and purification procedures: Tris-HCI buffer extraction, 70% ammonium sulfate fractionation, CM-rellulosr column chromatography, heat inactivation and Sephadex G-75 column chromatography. This fraction was further purified by Sepharose 4B and Sephadex G-150 column chromatographies. Three fractions obtained were subjected to Native-PAGE and SDS-PAGE using gradient gels and the silver staining method. Molecular weights of the native proteins and their subunits were estimated.

• Parasites, Hosts and Diseases
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• v.29 no.4
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• pp.389-396
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• 1991

Antibody changes in experimental anisakiasis were observed in 10 rabbits which were infected each with 10 Anisakis simplex larvae. The sera were collected before and on the 6th to the 95th day after the infection. Using crude saline extract of Anisakis larvae as antigen, specific IgM and IgG antibody levels were observed by ELISA and SDS-polyacrylamide gel electrophoresislimmunoblot. Levels of specific-IgM antibody were elevated from the 6th day, reached their peaks on the lIth day after the infection, and dropped thereafter. Serum levels of IgG antibody increased from the 6th day and reached their peak on the 26th day after the infection, and decreased gradually thereafter. When SDS-PAGE of the crude extract was done, at least forty-one SDS-polypeptide bands were recognized. Of them, IgM antibody reacted mainly to the bands of 168, 95, 74, 64, 51, 47 and 34 kDa while IgG antibody reacted strongly to 168, 92, 85, 64, 58, 52, 42 and 40 kDa bands. The crude extract showed negligible cross reactions with sera of other parasitic diseases and normal control. Key words: Anisakis simplex larvae, experimental anisakiasis, rabbit, antibody, ELISA, SDS- PAGE/immunoblot.

• Korean Journal of Food Science and Technology
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• v.30 no.1
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• pp.1-5
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• 1998

To find out the difference between native bee-honey (NBH) and foreign bee-honey (FBH), quantification of honey protein and investigation of specific protein in NBH were carried out by SDS-PAGE. Contents of honey protein in NBH and FBH were measured by Bradford and Lowry method. The contents of protein determined by Bradford method were $0.1{\sim}3.3\;mg/g$ in NBH and $0.2{\sim}1.6\;mg/g$ in FBH, and by Lowry method were $12.9{\sim}45.7\;mg/g$ in NBH and $15.8{\sim}27.1\;mg/g$ in FBH. In order to investigate the distribution of bee honey proteins, the SDS-PAGE was performed. The results showed that molecular weight of the major proteins in NBH and in FBH were 56 kDa and 59 kDa. respectively. Therefore, it was confirmed that the difference between NBH and FBH can be identified visually by SDS-PAGE analysis. The major proteins in NBH and FBH were purified through two step chromatography, and the obtained proteins were used as marker protein in SDS-PAGE to discriminate NBH and FBH.

• Korean Journal of Food Science and Technology
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• v.17 no.1
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• pp.1-4
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• 1985

For the systematic investigation of biochemical characteristics of Korean ginseng protein by years, protein fractions were analyzed by the techniques of polyacrylamide gel electrophoresis, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and gel filtration, while the amino acid composition was studied by amino acid autoanalyzer. Results of polyacrylamide gel electrophoresis and SDS-PAGE showed a few difference in pattern and number of bands depending on the age of the root. However, the number of bands obtained from polyacrylamide gel electrophoresis and SDS-PAGE was 8 and 7 to 11, respectively. When water extracted proteins were fractionated by Sephadex G-200, the main peak among 2 peaks was collected and lyophillized. Its mol. wt. was extimated to be 43,000 by the SDS-PAGE method. In amino acid composition of water extracted protein and main fraction of gel filtration, arginine content was the highest, 47.17% in water extracted protein and 57.36% in main fraction followed by glutamic acid and asparatic acid. On the contrary, cystine and methionine contents were very low in both cases.

• Biomolecules & Therapeutics
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• v.9 no.1
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• pp.7-14
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• 2001

The chicken meat has been reported as one of the food causing allergic reactions predominantly to Korean. At present, several in vitro tests for immunoglobulinG (IgG)-mediated as well as IgE-mediated food allergy are available. 13 clinically chicken meat-allergic patients were investigated together with 4control subjects for identification of chicken meat-specific reactivity by ELISA. Also, protein profile and IgE, IgGtotal and IgG4-reacting allergens were detected by means of sodium dodecyl sulfate-polyacrylamide gel electro-phoresis (SDS-PAGE)and immunoblotting. Chicken meat extracts were prepared as raw, heated, heat and simulated gastric fluid (SGF) treated samples to characterize the stability of allergen to physicochemical treatment. SDS-PAGE revealed 9~200 kDa bands. And in immunoblotting 7 sera were identified most major bands between 10 and 78 kDa. In case of IgE, six proteins (17, 26, 35, 40, 78 kDa) were predominant in heat-treated extract, and the one (35 kDa) was present in SGF-treated preparations. In case of IgG$_{total}$ and IgG4, most of them showed a patters simmilar to IgE. There were significant differences (P<0.05) in IgE, IgG$_{total}$ , IgG4 Abs to chicken meat between the allergic and control subjects in ELISA. In addition, the concentration of IgG4Abs in the challenge-positive subjects was significantly higher than that of control subjects. It is considered that the specific IgE response to chicken meat was rarely prevalent to Koreans. However, the specific IgG4 response play an important role in the development of allergic symptoms.

• Biomedical Science Letters
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• v.4 no.1
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• pp.73-76
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• 1998

The authors characterized the antigen proteins and some specific antibodies from Echinostoma hortense. Crude antigen extracted from E. hortense worm was analyzed by SDS-PAGE of the crude antigen showed 46 profiles between 200.2 - 8.2kDa, among which 200.2, 107.9, 86.8, 75, 69.8, 46.8, 43.5, 34.5, 20.9, 13.6, 12.6, 11.7, and 8.2kDa, protein profiles were strong. EITB resolved the specific IgG antibody into 17 profiles between 193 - 13.7kDa, among which 198, 123.4, 100.8, 91.1, 88.1, 62.8, 34.2, 32, 29.9, 18, 15.7, 13.7kDa profiles showed strong immunostain.

• The Korean Journal of Food And Nutrition
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• v.1 no.2
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• pp.50-55
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• 1988

B-Amylase was obtained from sweet potato extract in a crystalline state by dialysis against water after precipitated with acetone according to the method reported previously followed by DEAE Sephadex A-50 ion exchange chromatography plus gel chromatography of Sephadex G-200. The purified enzyme was homogeneous by SDS PAGE. The efforts had done to remove the miner bands in SDS PAGE by Sephadex G-200 gel chromatography, DATE Sephadex A-50 ion exchange chromatography. isoelectrophocusing, affinity chromatography, hydroxyapatite chromatography, recrystallizstion and HPLC on a column of TSK gel SW 3000 but have given any result. But, N -terminal amino acid of the enzyme was revealed mainly alanine and trace of glycine and glutamic acid. Therefore, it seems that the miner bands in SDS PAGE have a role of subunit.

• Preventive Nutrition and Food Science
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• v.12 no.2
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• pp.103-110
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• 2007

The protein profiles among Korean rice cultivars were assessed by total protein determination, solubility fractionation, SDS-PAGE analysis and scanning densitometry. In the extraction of protein, the SDS/urea system at a neutral pH was more efficient than that at alkaline pH. The determination of total protein showed that the protein content was similar among cultivars, ranging from 87.9 to 92.7 mg/g dry weight. Additionally, the water/NaCl-soluble protein fraction, containing 14${\sim}$16 kDa albumin and 22 kDa globulin ${\alpha}$-globulin, was also similar among cultivars, with a range of 9.94 to 11.98 mg/g dry weight. The SDS-PAGE/densitometry of total protein showed that there was no discernable difference in proteins of higher molecular weights among various cultivars, whereas the amount of lower molecular weight proteins (14${\sim}$16 kDa) is somewhat variable among cultivars. Furthermore, SDS-PAGE analysis of water/NaCl-soluble and propanol-soluble fractions indicates that there is a discernible change in the content of albumin, globulin or prolamin among cultivars. Thus, the PAGE/densitometry method, preceded by solubility fractionation, is useful for examining differences in protein profiles of rice cultivars.

• Journal of fish pathology
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• v.10 no.1
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• pp.31-38
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• 1997

Aeromonas hydrophila isolated from the intestine of carp produced several kinds of proteases into the medium. Inhibitor assay with the culture supernatant of A. hydrophila showed that there were major metalloproteases and minor serine proteases. Gelatin SDS-PAGE showed two proteolytic bands. One broad protease band was inhibited by metalloprotease specific inhibitor, EDTA, indicating a metalloprotease. The other was inhibited by serine protease specific inhibitor, PMSF, suggesting a serine protease. The proteolytic activities of both extracellular proteases remained on Gelatin SDS-PAGE after heating at $70^{\circ}C$ for 30 min. However, the major metalloprotease was separated into two proteolytic bands on Gelatin PAGE by gel filtration chromatography on Sephadex G-75.

• The Korean Journal of Zoology
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• v.36 no.2
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• pp.238-244
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• 1993

We identified juvenile hormone binding protein (JHBP) from last instar larval hemollvnph of Hvphantria cunea using gel filtration and non-SDS PAGE. Two kinds of JHBP in hemollnnph were found at two peaks by gel filtration (Sephadex G-100) and also at Rm values of 0.13 and 0.57 by non-SDS PAGE. JHBP was partially purified using anion exchange chromatosraphv, preparative gel filteration, and preparative PAGE. Dextrin coated charcoal (DCC) binding assay was employed to monitor the location of JHBP in chromatographic profile during the purification process. Purity of JHBP was checked by silver staining of 1091 SDS-Polyacrvlamide.